Phosphorylation of LAT by p-SYK

Stable Identifier
Reaction [transition]
Homo sapiens
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LAT is palmitoylated and membrane-associated adaptor protein. It rapidly becomes tyrosine-phosphorylated upon receptor engagement. LAT has nine conserved tyrosine residues of which five have been shown to undergo phosphorylation (Y127, Y132, Y171, Y191 and Y226). Src family kinases, SYK and ZAP-70 efficiently phosphorylate LAT on these tyrosine residues (Jiang & Cheng 2007, Paz et al. 2001). Phosphorylation of LAT creates binding sites for the Src homology 2 (SH2) domain proteins PLC-gamma1, GRB2 and GADS, which indirectly bind SOS, VAV, SLP-76 and ITK (Wange 2000).
Literature References
PubMed ID Title Journal Year
10072481 Cutting edge: a role for the adaptor protein LAT in human NK cell-mediated cytotoxicity

Samelson, LE, Irvin, BJ, Abraham, RT, Dick, CJ, Leibson, PJ, Billadeau, DD, Zhang, W, Jevremovic, D, Schoon, RA

J. Immunol. 1999
11368773 Mapping the Zap-70 phosphorylation sites on LAT (linker for activation of T cells) required for recruitment and activation of signalling proteins in T cells

Abo, A, Wang, S, Lu, X, Paz, PE, Stokoe, D, Clarke, H

Biochem. J. 2001
16938345 Evidence of LAT as a dual substrate for Lck and Syk in T lymphocytes

Jiang, Y, Cheng, H

Leuk Res 2007
Catalyst Activity

protein tyrosine kinase activity of DAP12 Receptors:p-DAP12:p-6Y-SYK [plasma membrane]

Orthologous Events
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